Q92522 (H1X_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H1x

Gene names

Name:

H1FX

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histones H1 are necessary for the condensation of nucleosome chains into higher order structures.
Subcellular location	Nucleus. Chromosome.
Tissue specificity	Expressed ubiquitously.
Sequence similarities	Belongs to the histone H1/H5 family. Contains 1 H15 (linker histone H1/H5 globular) domain.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nucleosome assembly Non-traceable author statement. Source: UniProtKB
Cellular component	nucleosome Non-traceable author statement. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 213	212	Histone H1x		PRO_0000195912
Regions
	Domain	44 – 118	75	H15
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.3
	Modified residue	2	1	Phosphoserine Ref.5
	Modified residue	31	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
	Modified residue	33	1	Phosphoserine Ref.8
	Modified residue	47	1	N6-acetyllysine Ref.12
	Modified residue	179	1	N6-acetyllysine Ref.12
	Modified residue	180	1	N6-acetyllysine Ref.12
	Modified residue	182	1	N6-acetyllysine Ref.12
	Modified residue	185	1	N6-acetyllysine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Q92522 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 11548D85C5448FF2	FASTA	213	22,487
	10 20 30 40 50 60 MSVELEEALP VTTAEGMAKK VTKAGGSAAL SPSKKRKNSK KKNQPGKYSQ LVVETIRRLG 70 80 90 100 110 120 ERNGSSLAKI YTEAKKVPWF DQQNGRTYLK YSIKALVQND TLLQVKGTGA NGSFKLNRKK 130 140 150 160 170 180 LEGGGERRGA PAAATAPAPT AHKAKKAAPG AAGSRRADKK PARGQKPEQR SHKKGAGAKK 190 200 210 DKGGKAKKTA AAGGKKVKKA AKPSVPKVPK GRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the cDNA encoding a novel subtype of histone H1." Yamamoto T., Horikoshi M. Gene 173:281-285(1996) [PubMed: 8964515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[3]	Bienvenut W.V., Calvo F., Kolch W. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-19; 48-57; 76-86; 95-118 AND 128-143, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[4]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-33, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-179; LYS-180; LYS-182 AND LYS-185, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D64142 mRNA. Translation: BAA11018.1. BC000426 mRNA. Translation: AAH00426.1. BC010435 mRNA. Translation: AAH10435.1.
IPI	IPI00021924.
PIR	JC4928.
RefSeq	NP_006017.1. NM_006026.3.
UniGene	Hs.75307.
3D structure databases
ProteinModelPortal	Q92522.
SMR	Q92522. Positions 44-118.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92522. 8 interactions.
MINT	MINT-5009259.
STRING	Q92522.
PTM databases
PhosphoSite	Q92522.
Polymorphism databases
DMDM	6016184.
Proteomic databases
PeptideAtlas	Q92522.
PRIDE	Q92522.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000333762; ENSP00000329662; ENSG00000184897.
GeneID	8971.
KEGG	hsa:8971.
UCSC	uc003elx.1. human.
Organism-specific databases
CTD	8971.
GeneCards	GC03M129033.
H-InvDB	HIX0018256.
HGNC	HGNC:4722. H1FX.
HPA	CAB012235.
MIM	602785. gene.
neXtProt	NX_Q92522.
PharmGKB	PA29099.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20375.
GeneTree	ENSGT00550000074201.
HOGENOM	HBG446956.
HOVERGEN	HBG009035.
InParanoid	Q92522.
OMA	SLAKIYT.
OrthoDB	EOG4TF0MQ.
PhylomeDB	Q92522.
Gene expression databases
ArrayExpress	Q92522.
Bgee	Q92522.
CleanEx	HS_H1FX.
Genevestigator	Q92522.
GermOnline	ENSG00000184897. Homo sapiens.
Family and domain databases
InterPro	IPR005818. Histone_H1/H5. IPR005819. Histone_H5. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K11275.
Pfam	PF00538. Linker_histone. 1 hit. [Graphical view]
PRINTS	PR00624. HISTONEH5.
SMART	SM00526. H15. 1 hit. [Graphical view]
PROSITE	PS51504. H15. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	33663.
SOURCE	Search...

Entry information

Entry name

H1X_HUMAN

Accession

Primary (citable) accession number: Q92522

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.